The amino acid conjugate formed by the interaction of the anion transport inhibitor 4,4'-diisothiocyano-2,2'-stilbenedisulfonic acid (DIDS) with band 3 protein from human red blood cell membranes.
The specific anion transport inhibitor 4,4'-diisothiocyano-2,2'-stilbenedisulfonic acid (DIDS) and its reduced analog (H2DIDS), when irreversibly bound to band 3 protein of the red blood cell membrane, form amino acid conjugates through interaction with the epsilon-amino group of a particular lysine residue. The specific residue is located in a transmembrane segment of band 3 protein and appears to be a close neighbor of the transport site.
D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid / Q000031:analogs & derivatives; D012856:4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid / Q000031:analogs & derivatives / Q000097:blood*; D001457:Anion Exchange Protein 1, Erythrocyte; D001120:Arginine / Q000378:metabolism; D001692:Biological Transport; D001798:Blood Proteins / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D002855:Chromatography, Thin Layer; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D008239:Lysine / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D013267:Stilbenes / Q000097:blood*
D001457:Anion Exchange Protein 1, Erythrocyte; D001798:Blood Proteins; D008565:Membrane Proteins; D013267:Stilbenes; D012856:4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; C018564:dihydro-DIDS; D001120:Arginine; D008239:Lysine; D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid